Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu

Autores
Barrantes, Francisco José
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina
Fil: Barrantes, Francisco José. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Abstract: Hampered by the diffraction phenomenon, as expressed in 1873 by Abbe, applications of optical microscopy to image biological structures were for a long time limited to resolutions above the ~200 nm barrier and restricted to the observation of stained specimens. The introduction of fluorescence was a game changer, and since its inception it became the gold standard technique in biological microscopy. The plasma membrane is a tenuous envelope of 4 nm–10 nm in thickness surrounding the cell. Because of its highly versatile spectroscopic properties and availability of suitable instrumentation, fluorescence techniques epitomize the current approach to study this delicate structure and its molecular constituents. The wide spectral range covered by fluorescence, intimately linked to the availability of appropriate intrinsic and extrinsic probes, provides the ability to dissect membrane constituents at the molecular scale in the spatial domain. In addition, the time resolution capabilities of fluorescence methods provide complementary high precision for studying the behavior of membrane molecules in the time domain. This review illustrates the value of various fluorescence techniques to extract information on the topography and motion of plasma membrane receptors. To this end I resort to a paradigmatic membrane-bound neurotransmitter receptor, the nicotinic acetylcholine receptor (nAChR). The structural and dynamic picture emerging from studies of this prototypic pentameric ligand-gated ion channel can be extrapolated not only to other members of this superfamily of ion channels but to other membrane-bound proteins. I also briefly discuss the various emerging techniques in the field of biomembrane labeling with new organic chemistry strategies oriented to applications in fluorescence nanoscopy, the form of fluorescence microscopy that is expanding the depth and scope of interrogation of membrane-associated phenomena.
Fuente
Frontiers in Molecular Biosciences. 2022, 9:1014659
Materia
MEMBRANA PLASMATICA
INTERACCIONES PROTEÍNA-PROTEÍNA
COLESTEROL
NANOSCOPIA
MICROSCOPIO FLUORESCENTE
RECEPTOR DE ACETILCOLINA
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
Repositorio Institucional (UCA)
Institución
Pontificia Universidad Católica Argentina
OAI Identificador
oai:ucacris:123456789/18149

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oai_identifier_str oai:ucacris:123456789/18149
network_acronym_str RIUCA
repository_id_str 2585
network_name_str Repositorio Institucional (UCA)
spelling Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieuBarrantes, Francisco JoséMEMBRANA PLASMATICAINTERACCIONES PROTEÍNA-PROTEÍNACOLESTEROLNANOSCOPIAMICROSCOPIO FLUORESCENTERECEPTOR DE ACETILCOLINAFil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; ArgentinaFil: Barrantes, Francisco José. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaAbstract: Hampered by the diffraction phenomenon, as expressed in 1873 by Abbe, applications of optical microscopy to image biological structures were for a long time limited to resolutions above the ~200 nm barrier and restricted to the observation of stained specimens. The introduction of fluorescence was a game changer, and since its inception it became the gold standard technique in biological microscopy. The plasma membrane is a tenuous envelope of 4 nm–10 nm in thickness surrounding the cell. Because of its highly versatile spectroscopic properties and availability of suitable instrumentation, fluorescence techniques epitomize the current approach to study this delicate structure and its molecular constituents. The wide spectral range covered by fluorescence, intimately linked to the availability of appropriate intrinsic and extrinsic probes, provides the ability to dissect membrane constituents at the molecular scale in the spatial domain. In addition, the time resolution capabilities of fluorescence methods provide complementary high precision for studying the behavior of membrane molecules in the time domain. This review illustrates the value of various fluorescence techniques to extract information on the topography and motion of plasma membrane receptors. To this end I resort to a paradigmatic membrane-bound neurotransmitter receptor, the nicotinic acetylcholine receptor (nAChR). The structural and dynamic picture emerging from studies of this prototypic pentameric ligand-gated ion channel can be extrapolated not only to other members of this superfamily of ion channels but to other membrane-bound proteins. I also briefly discuss the various emerging techniques in the field of biomembrane labeling with new organic chemistry strategies oriented to applications in fluorescence nanoscopy, the form of fluorescence microscopy that is expanding the depth and scope of interrogation of membrane-associated phenomena.Frontiers Media2022info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://repositorio.uca.edu.ar/handle/123456789/1814910.3389/fmolb.2022.1014659Barrantes, F. J. Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu [en línea]. Frontiers in Molecular Biosciences. 2022, 9:1014659. doi: 10.3389/fmolb.2022.1014659. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/18149Frontiers in Molecular Biosciences. 2022, 9:1014659reponame:Repositorio Institucional (UCA)instname:Pontificia Universidad Católica Argentinaenginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/4.0/2025-07-03T10:59:48Zoai:ucacris:123456789/18149instacron:UCAInstitucionalhttps://repositorio.uca.edu.ar/Universidad privadaNo correspondehttps://repositorio.uca.edu.ar/oaiclaudia_fernandez@uca.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:25852025-07-03 10:59:48.218Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentinafalse
dc.title.none.fl_str_mv Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu
title Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu
spellingShingle Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu
Barrantes, Francisco José
MEMBRANA PLASMATICA
INTERACCIONES PROTEÍNA-PROTEÍNA
COLESTEROL
NANOSCOPIA
MICROSCOPIO FLUORESCENTE
RECEPTOR DE ACETILCOLINA
title_short Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu
title_full Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu
title_fullStr Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu
title_full_unstemmed Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu
title_sort Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu
dc.creator.none.fl_str_mv Barrantes, Francisco José
author Barrantes, Francisco José
author_facet Barrantes, Francisco José
author_role author
dc.subject.none.fl_str_mv MEMBRANA PLASMATICA
INTERACCIONES PROTEÍNA-PROTEÍNA
COLESTEROL
NANOSCOPIA
MICROSCOPIO FLUORESCENTE
RECEPTOR DE ACETILCOLINA
topic MEMBRANA PLASMATICA
INTERACCIONES PROTEÍNA-PROTEÍNA
COLESTEROL
NANOSCOPIA
MICROSCOPIO FLUORESCENTE
RECEPTOR DE ACETILCOLINA
dc.description.none.fl_txt_mv Fil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina
Fil: Barrantes, Francisco José. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Abstract: Hampered by the diffraction phenomenon, as expressed in 1873 by Abbe, applications of optical microscopy to image biological structures were for a long time limited to resolutions above the ~200 nm barrier and restricted to the observation of stained specimens. The introduction of fluorescence was a game changer, and since its inception it became the gold standard technique in biological microscopy. The plasma membrane is a tenuous envelope of 4 nm–10 nm in thickness surrounding the cell. Because of its highly versatile spectroscopic properties and availability of suitable instrumentation, fluorescence techniques epitomize the current approach to study this delicate structure and its molecular constituents. The wide spectral range covered by fluorescence, intimately linked to the availability of appropriate intrinsic and extrinsic probes, provides the ability to dissect membrane constituents at the molecular scale in the spatial domain. In addition, the time resolution capabilities of fluorescence methods provide complementary high precision for studying the behavior of membrane molecules in the time domain. This review illustrates the value of various fluorescence techniques to extract information on the topography and motion of plasma membrane receptors. To this end I resort to a paradigmatic membrane-bound neurotransmitter receptor, the nicotinic acetylcholine receptor (nAChR). The structural and dynamic picture emerging from studies of this prototypic pentameric ligand-gated ion channel can be extrapolated not only to other members of this superfamily of ion channels but to other membrane-bound proteins. I also briefly discuss the various emerging techniques in the field of biomembrane labeling with new organic chemistry strategies oriented to applications in fluorescence nanoscopy, the form of fluorescence microscopy that is expanding the depth and scope of interrogation of membrane-associated phenomena.
description Fil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina
publishDate 2022
dc.date.none.fl_str_mv 2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://repositorio.uca.edu.ar/handle/123456789/18149
10.3389/fmolb.2022.1014659
Barrantes, F. J. Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu [en línea]. Frontiers in Molecular Biosciences. 2022, 9:1014659. doi: 10.3389/fmolb.2022.1014659. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/18149
url https://repositorio.uca.edu.ar/handle/123456789/18149
identifier_str_mv 10.3389/fmolb.2022.1014659
Barrantes, F. J. Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu [en línea]. Frontiers in Molecular Biosciences. 2022, 9:1014659. doi: 10.3389/fmolb.2022.1014659. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/18149
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/4.0/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/4.0/
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Frontiers Media
publisher.none.fl_str_mv Frontiers Media
dc.source.none.fl_str_mv Frontiers in Molecular Biosciences. 2022, 9:1014659
reponame:Repositorio Institucional (UCA)
instname:Pontificia Universidad Católica Argentina
reponame_str Repositorio Institucional (UCA)
collection Repositorio Institucional (UCA)
instname_str Pontificia Universidad Católica Argentina
repository.name.fl_str_mv Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentina
repository.mail.fl_str_mv claudia_fernandez@uca.edu.ar
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